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Flexible flap regions

NMR is unique in that it can provide detailed and specific information on molecular dynamics in addition to structural information. The use of relaxation time measurements allows the relative mobility of individual atomic positions within a macromolecule to be determined. The d3mamic information obtained includes not only the rates or frequencies of internal motions but also their amplitudes. Such amplitudes are often expressed by order parameters. Not surprisingly, it is observed in many cases that the termini of proteins are more flexible than internal regions. More interestingly, NMR has provided a number of examples where internal loops in proteins have been shown to have dynamics that may be associated with their function. A good example of this is HIV protease, where NMR studies have identified reduced-order parameters in the flap region of the molecule that may reflect flexibility to allow entry of substrates or inhibitors into the active site. [Pg.533]


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See also in sourсe #XX -- [ Pg.55 ]




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